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Literature summary for 3.2.1.4 extracted from

  • Ichikawa, S.; Yoshida, M.; Karita, S.; Kondo, M.; Goto, M.
    Carbohydrate-binding modules influence substrate specificity of an endoglucanase from Clostridium thermocellum (2016), Biosci. Biotechnol. Biochem., 80, 188-192 .
    View publication on PubMed
Search for more literature for 3.2.1.4

Application

Application Comment Organism
degradation replacement of carbohydrate-binding module by modules from enzymes with different specificities leads to enhanced activity that is affected by carbohydrate-binding module binding specificity, e.g. on ball-milled cellulose or avicel. The chimeric enzymes can efficiently degrade milled lignocellulosic materials, such as corn hulls Acetivibrio thermocellus

Protein Variants

Protein Variants Comment Organism
additional information replacement of carbohydrate-binding module either with a family 3 microcrystalline cellulose-directed carbohydrate-binding module from Clostridium josui scaffoldin, or a family 6 xylan-directed carbohydrate-binding module from Clostridium stercorarium xylanase 11A. Chimeric endoglucanases show enhanced activity that is affected by carbohydrate-binding module binding specificity. The chimeric enzymes can efficiently degrade milled lignocellulosic materials, such as corn hulls Acetivibrio thermocellus

Organism

Organism UniProt Comment Textmining
Acetivibrio thermocellus
-
-
-
Acetivibrio thermocellus 132
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carboxymethylcellulose + H2O
-
 Acetivibrio thermocellus ?
-
 ?
carboxymethylcellulose + H2O
-
 Acetivibrio thermocellus 132 ?
-
 ?

Synonyms

Synonyms Comment Organism
Cel5E
-
 Acetivibrio thermocellus